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Database: UniProt
Entry: R7CA17_9CLOT
LinkDB: R7CA17_9CLOT
Original site: R7CA17_9CLOT 
ID   R7CA17_9CLOT            Unreviewed;       240 AA.
AC   R7CA17;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=RNA-binding protein KhpB {ECO:0000256|HAMAP-Rule:MF_00867};
DE   AltName: Full=RNA-binding protein EloR {ECO:0000256|HAMAP-Rule:MF_00867};
GN   Name=khpB {ECO:0000256|HAMAP-Rule:MF_00867};
GN   Synonyms=eloR {ECO:0000256|HAMAP-Rule:MF_00867};
GN   ORFNames=BN737_00451 {ECO:0000313|EMBL:CDD74168.1};
OS   Clostridium sp. CAG:62.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262828 {ECO:0000313|EMBL:CDD74168.1, ECO:0000313|Proteomes:UP000018137};
RN   [1] {ECO:0000313|EMBL:CDD74168.1, ECO:0000313|Proteomes:UP000018137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:62 {ECO:0000313|Proteomes:UP000018137};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: A probable RNA chaperone. Forms a complex with KhpA which
CC       binds to cellular RNA and controls its expression. Plays a role in
CC       peptidoglycan (PG) homeostasis and cell length regulation.
CC       {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- SUBUNIT: Forms a complex with KhpA. {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- DOMAIN: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH
CC       and R3H). {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- SIMILARITY: Belongs to the KhpB RNA-binding protein family.
CC       {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00867}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDD74168.1}.
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DR   EMBL; CBHQ010000078; CDD74168.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7CA17; -.
DR   Proteomes; UP000018137; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd02414; KH-II_Jag; 1.
DR   CDD; cd02644; R3H_jag; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.30.30.80; probable RNA-binding protein from clostridium symbiosum atcc 14940; 1.
DR   Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR   HAMAP; MF_00867; KhpB; 1.
DR   InterPro; IPR038008; Jag_KH.
DR   InterPro; IPR038247; Jag_N_dom_sf.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR039247; KhpB.
DR   InterPro; IPR032782; KhpB_N.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR034079; R3H_KhpB.
DR   NCBIfam; NF041568; Jag_EloR; 1.
DR   PANTHER; PTHR35800; PROTEIN JAG; 1.
DR   PANTHER; PTHR35800:SF1; RNA-BINDING PROTEIN KHPB; 1.
DR   Pfam; PF14804; Jag_N; 1.
DR   Pfam; PF13083; KhpA-B_KH; 1.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM01245; Jag_N; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF82708; R3H domain; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   3: Inferred from homology;
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_00867};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00867};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00867};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00867};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018137};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00867}.
FT   DOMAIN          142..208
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   REGION          215..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   240 AA;  28208 MW;  DE51EF0C6D800DC3 CRC64;
     MEEWKEFSAK TADEALTNAL IQMETTSDQI EYEVVEEEKS GILGLFSKPA VIRVRKKENV
     VDTVKNFLAK TFQAMKLDVE IETEFDEVEN EIRIELKGTE MGMLIGKRGQ TLDSLQYLTS
     LVANKNKDTY TKIKIDTENY RQRRKETIEN LARNVASKVK KTGRPAFLEP MNPYERRIIH
     AELQADKYVD THSEGEEPHR KVVITLNREF ASELPRRNNY RRRNNNYSRD RKRPYQEKKD
//
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